The S100 family of EF-hand calcium (Ca2+)-binding proteins is essential for a wide range of cellular functions. During infection, certain S100 proteins act as damage-associated molecular patterns (DAMPs) and interact with pattern recognition receptors to modulate inflammatory responses. In addition, these inflammatory S100 proteins have potent antimicrobial properties and are essential components of the immune response to invading pathogens. In this review, we focus on S100 proteins that exhibit antimicrobial properties through the process of metal limitation, termed nutritional immunity, and discuss several recent advances in our understanding of S100 protein-mediated metal sequestration at the site of infection.
Nutritional Immunity: S100 Proteins at the Host-Pathogen Interface*
J. Zackular,W. Chazin,Eric P. Skaar
Published 2015 in Journal of Biological Chemistry
ABSTRACT
PUBLICATION RECORD
- Publication year
2015
- Venue
Journal of Biological Chemistry
- Publication date
2015-06-08
- Fields of study
Biology, Medicine
- Identifiers
- External record
- Source metadata
Semantic Scholar, PubMed
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